We have established that Beta-lysine (3,6-diaminohexanoate) is degraded by a Pseudomonas sp. That first enzymatic step is the acetylation of the amino group in the 6-position; the second step is a transamination between 6-acetamido-hexanoate and alpha-ketoglutarate to form 3-keto-6-acetamidohexanoate and glutamate. The further degradation of the Beta-keto acid is stimulated by the addition of acetyl-CoA, but the nature of the reaction and the products formed have not been determined. We plan to investigate this process in order to identify the products and characterize the enzymatic system. We further propose to identify subsequent enzymatic steps in the degradation of Beta-lysine that involve new or little known reactions and compounds. We plan also to complete earlier studies on the specificity and some other properties of the CoA transferase from Clostridium SB4 and to determine whether the degradation of 3-keto-5-aminohexanoate (KAH) by an aerobic Brevibacterium sp. involves the participation of a KAH cleavage enzyme similar to that in lysine-fermenting clostridia.